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B4TU42 (TYPH_SALSV) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thymidine phosphorylase

EC=2.4.2.4
Alternative name(s):
TdRPase
Gene names
Name:deoA
Ordered Locus Names:SeSA_A4822
OrganismSalmonella schwarzengrund (strain CVM19633) [Complete proteome] [HAMAP]
Taxonomic identifier439843 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length440 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis By similarity. HAMAP-Rule MF_01628

Catalytic activity

Thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate. HAMAP-Rule MF_01628

Pathway

Pyrimidine metabolism; dTMP biosynthesis via salvage pathway; dTMP from thymine: step 1/2. HAMAP-Rule MF_01628

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01628

Sequence similarities

Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 440440Thymidine phosphorylase HAMAP-Rule MF_01628
PRO_1000186272

Sequences

Sequence LengthMass (Da)Tools
B4TU42 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: D33E999347848375

FASTA44047,018
        10         20         30         40         50         60 
MFLAQEIIRK KRDGHALSDE EIRFFINGIR DNTISEGQIA ALAMTIFFHD MTMPERVSLT 

        70         80         90        100        110        120 
MAMRDSGSVL DWKSLNLNGP IVDKHSTGGV GDVTSLMLGP MVAACGGYVP MISGRGLGHT 

       130        140        150        160        170        180 
GGTLDKLEAI PGFDIFPDDN RFREIIQDVG VAIIGQTSSL APADKRFYAT RDITATVDSI 

       190        200        210        220        230        240 
PLITGSILAK KLAEGLDALV MDVKVGSGAF MPTYELSEAL AEAIVGVANG AGVRTTALLT 

       250        260        270        280        290        300 
DMNQVLASSA GNAVEVREAV QFLTGEYRNP RLFDVTMALC VEMLISGQLA KDDAEARAKL 

       310        320        330        340        350        360 
QAVLDNGKAA EVFGRMVAAQ KGPSDFVENY DKYLPTAMLS KAVYADTEGF ISAMDTRALG 

       370        380        390        400        410        420 
MAVVSMGGGR RQASDTIDYS VGFTDMARLG DSIDGQRPLA VIHAKDETSW QEAAKAVKAA 

       430        440 
IILDDKAPAS TPSVYRRITE 

« Hide

References

[1]"Comparative genomics of 28 Salmonella enterica isolates: evidence for CRISPR-mediated adaptive sublineage evolution."
Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., Leclerc J.E., Ravel J., Cebula T.A.
J. Bacteriol. 193:3556-3568(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CVM19633.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001127 Genomic DNA. Translation: ACF89038.1.
RefSeqYP_002117483.1. NC_011094.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING439843.SeSA_A4822.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF89038; ACF89038; SeSA_A4822.
PATRIC32378200. VBISalEnt87589_4772.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0213.
HOGENOMHOG000047313.
OMAFINGVRD.
OrthoDBEOG61ZTGG.

Enzyme and pathway databases

BioCycSENT439843:GHHR-431-MONOMER.
UniPathwayUPA00578; UER00638.

Family and domain databases

Gene3D3.40.1030.10. 1 hit.
3.90.1170.30. 1 hit.
HAMAPMF_01628. Thymid_phosp.
InterProIPR000312. Glycosyl_Trfase_fam3.
IPR017459. Glycosyl_Trfase_fam3_N_dom.
IPR013102. PYNP_C.
IPR018090. Pyrmidine_PPas_bac/euk.
IPR000053. Pyrmidine_PPase.
IPR017872. Pyrmidine_PPase_CS.
IPR013465. Thymidine_Pase.
[Graphical view]
PANTHERPTHR10515. PTHR10515. 1 hit.
PfamPF02885. Glycos_trans_3N. 1 hit.
PF00591. Glycos_transf_3. 1 hit.
PF07831. PYNP_C. 1 hit.
[Graphical view]
PIRSFPIRSF000478. TP_PyNP. 1 hit.
SMARTSM00941. PYNP_C. 1 hit.
[Graphical view]
SUPFAMSSF47648. SSF47648. 1 hit.
SSF52418. SSF52418. 1 hit.
SSF54680. SSF54680. 1 hit.
TIGRFAMsTIGR02643. T_phosphoryl. 1 hit.
TIGR02644. Y_phosphoryl. 1 hit.
PROSITEPS00647. THYMID_PHOSPHORYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTYPH_SALSV
AccessionPrimary (citable) accession number: B4TU42
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: September 23, 2008
Last modified: July 9, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways